Abstract
As a prelude to experimental and theoretical work on the mechanical properties of fibrillar beta-lactoglobulin gels, this paper reports the structural characterization of beta-lactoglobulin fibrils by electron and atomic force microscopy (AFM), infrared and Raman spectroscopy, and powder X-ray diffraction. Aggregates formed by incubation of beta-lactoglobulin in various alcohol-water mixtures at pH 2, and in water-trifluoroethanol (TFE) at pH 7, were found to be wormlike (similar to7 nm in width and 1 mum in length), smoother, and seemingly stiffer fibrils formed on heating aqueous beta-lactoglobulin solutions at pH 2 and low ionic strength, although there was little evidence for the higher-order structures common in most amyloid-forming systems. Time-lapse AFM also revealed differences in the formation of these two fibril types: thermally induced aggregation occurring more cooperatively, in keeping with a nucleation and growth process. Only short stiff-rods (
| Original language | English |
|---|---|
| Pages (from-to) | 2408 - 2419 |
| Number of pages | 12 |
| Journal | BIOMACROMOLECULES |
| Volume | 5 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Nov 2004 |
Fingerprint
Dive into the research topics of 'Fibrillar ß-lactoglobulin gels: Part 1. Fibril formation and structure'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver